Acyltransferasen

Acyltransferasen, or acyltransferases, are enzymes that catalyze the transfer of acyl groups (R-CO–) from a donor to an acceptor, producing esters, amides, or thioesters. The most common acyl donor is an acyl-CoA thioester, but other donors such as acyl-ACP or acyl phosphates are used in specialized pathways. Acceptors can be alcohols, amines, sugars, or other acyl groups, leading to a broad range of products including fatty acid esters and glycerophospholipids. Consequently, acyltransferases play central roles in lipid metabolism, membrane biosynthesis, protein modification, and the biosynthesis of natural products.

In biochemistry and cell biology, acyltransferases are typically classified as EC 2.3.x.x, transferases that move acyl groups. Major subfamilies include glycerol-3-phosphate acyltransferases (GPATs) and lysophosphatidic acid acyltransferases (LPAATs) involved in phospholipid biosynthesis, acyl-CoA cholesterol acyltransferases (ACATs) that form cholesterol esters, and N-myristoyltransferases (NMTs) that attach fatty acyl groups to proteins during or after translation. Other acyltransferases participate in natural product biosynthesis, detoxification, and post-translational modification of proteins, including S-acyltransferases such as the DHHC family that catalyze the reversible palmitoylation of cysteine residues.

Biological and medical relevance varies by enzyme. ACAT inhibitors have been explored in clinical contexts for cardiovascular risk reduction, though outcomes have been mixed. NMT inhibitors are being researched as potential anticancer agents. Structural and kinetic studies of acyltransferases continue to illuminate substrate specificity and guide enzyme engineering for industrial or therapeutic applications.